Exam 4: Proteins: Three-Dimensional Structure and Function
Exam 1: Introduction to Biochemistry72 Questions
Exam 2: Water94 Questions
Exam 3: Amino Acids and the Primary Structures of Proteins107 Questions
Exam 4: Proteins: Three-Dimensional Structure and Function116 Questions
Exam 5: Properties of Enzymes91 Questions
Exam 6: Mechanisms of Enzymes88 Questions
Exam 7: Coenzymes and Vitamins93 Questions
Exam 8: Carbohydrates92 Questions
Exam 9: Lipids and Membranes95 Questions
Exam 10: Introduction to Metabolism87 Questions
Exam 11: Glycolysis88 Questions
Exam 12: Gluconeogenesis, the Pentose Phosphate Pathway, and Glycogen Metabolism90 Questions
Exam 13: The Citric Acid Cycle93 Questions
Exam 14: Electron Transport and Atp Synthesis95 Questions
Exam 15: Photosynthesis89 Questions
Exam 16: Lipid Metabolism89 Questions
Exam 17: Amino Acid Metabolism84 Questions
Exam 18: Nucleotide Metabolism81 Questions
Exam 19: Nucleic Acids95 Questions
Exam 20: DNA Replication, repair, and Recombination89 Questions
Exam 21: Transcription and RNA Processing91 Questions
Exam 22: Protein Synthesis99 Questions
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The porphyrin prosthetic group is held into the interior of globin molecules by covalent bonds to specific amino acid residues.
(True/False)
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Proteins often consist of multiple subunits so that they may have different functions under different conditions.
(True/False)
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How many monomers are there in an oligomeric protein designated αβ2γ2?
(Multiple Choice)
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The amino acid that destabilizes alpha-helical structures and is usually found at the ends of alpha helices is
(Multiple Choice)
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________ received a Nobel Prize in 1964 for determining the structure of vitamin B12.He/she also solved the structure of penicillin in 1947 and developed many techniques used in the study of large proteins.
(Multiple Choice)
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Computers are used to advance the understanding of three-dimensional protein structure by
(Multiple Choice)
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A change from one conformation of a molecule to another involves ________.
(Multiple Choice)
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The conformation of the backbone of a polypeptide is described completely by the angle(s)of rotation about which bond(s)?
(Multiple Choice)
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The ________ is the single shape a protein adopts under physiological conditions.
(Multiple Choice)
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The amount of energy required to denature a protein is often small.
(True/False)
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Supersecondary structures that contain recognizable combinations of α-helices,β-strands and loops (e.g.the Greek Key)are called ________.
(Multiple Choice)
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Disulfide bond formation between two cysteine residues appropriately located in a polypeptide chain drives protein folding into the proper configuration.
(True/False)
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The principle forces holding subunits of an oligomeric protein to each other are ________.
(Multiple Choice)
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Ascorbic acid is necessary for the formation of hydroxyproline and hydroxylysine residues before they are incorporated into the collagen protein molecule.
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